?Cooking Eggs?

I really like meringues - quick to make, keep for a long time, taste great and an easy way to get some extra protein.

Now, I have read all over that cooking eggs ,the typical morning meal of 10 eggwhites, does not affect the protein, so you cook 30 grams of protein worth you get 30 grams. Does anyone know if the process of making meringues (baking for 1 hour at 300 degrees) affects the protein, making it useless?

Thanks
BB

well supposedly cooking food in any way somewhat denatures protein, however i wouldnt let it keep you up at night because all of us cook our food and we make progress, so i dont think baking your meringues is gonna kill you.

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Originally Posted by bigsd67

well supposedly cooking food in any way somewhat denatures protein, however i wouldnt let it keep you up at night because all of us cook our food and we make progress, so i dont think baking your meringues is gonna kill you.

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cooking protein does denature protein...this really doesn't have *that* big of an effect on our ability to assimilate the protein though...don't worry about it, eat up!

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Originally Posted by cb25

cooking protein does denature protein...this really doesn't have *that* big of an effect on our ability to assimilate the protein though...don't worry about it, eat up!

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basically what i was trying to convey...thanks for clarifying.

As the other guys have said when you denature something you just change its native conformation, not it's ability to be used in the body. The most basic level of protein structure, called the primary structure, is the linear sequence of amino acids. Different sequences of the acids along a chain, however, affect the structure of a protein molecule in different ways. Forces such as hydrogen bonds, disulfide bridges, attractions between positive and negative charges, and hydrophobic ("water-fearing") and hydrophilic ("water-loving") linkages cause a protein molecule to coil or fold into a secondary structure, examples of which are the so-called alpha helix and the beta pleated sheet. When forces cause the molecule to become even more compact, as in globular proteins, a tertiary protein structure is formed. When a protein is made up of more than one polypeptide chain, as in hemoglobin and some enzymes, it is said to have a quaternary structure. Hope that sheds a little light on structure and etc...

ahhhhhhhhhhhhhhhh!!!!!!! no more biochemistry!!!!!!!!!!!!!!!

:lol: sorry, just had flashbacks from last semester when i read that...

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Originally Posted by daman1

As the other guys have said when you denature something you just change its native conformation, not it's ability to be used in the body. The most basic level of protein structure, called the primary structure, is the linear sequence of amino acids. Different sequences of the acids along a chain, however, affect the structure of a protein molecule in different ways. Forces such as hydrogen bonds, disulfide bridges, attractions between positive and negative charges, and hydrophobic ("water-fearing") and hydrophilic ("water-loving") linkages cause a protein molecule to coil or fold into a secondary structure, examples of which are the so-called alpha helix and the beta pleated sheet. When forces cause the molecule to become even more compact, as in globular proteins, a tertiary protein structure is formed. When a protein is made up of more than one polypeptide chain, as in hemoglobin and some enzymes, it is said to have a quaternary structure. Hope that sheds a little light on structure and etc...

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All proteins are digested into peptides or individual AA before absorption so it makes no difference if the protein is denatured or not.

well then i pose this question...i've heard from some people that drinking RTD drinks is somewhat useless cuz of the protein in them being pastuerized...now i dont drink them on a regular basis cuz they're pricey, but if im traveling they come in handy so i guess it's ok to drink them and get all the quality protein?